eF-site ID 4z66-ABCDEFGH
PDB Code 4z66
Chain A, B, C, D, E, F, G, H

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Title Nucleosome disassembly by RSC and SWI/SNF is enhanced by H3 acetylation near the nucleosome dyad axis
Classification STRUCTURAL PROTEIN/DNA
Compound Histone H3.2
Source Xenopus laevis (African clawed frog) (4Z66)
Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPXDIQLARRIRGERA
B:  DNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLE
NVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLPKKT
D:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE
RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV
SEGTKAVTKYTSAK
E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV
TIMPXDIQLARRIRGERA
F:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF
GG
G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA
VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL
NKLLGRVTIAQGGVLPNIQSVLLPKK
H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE
RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV
SEGTKAVTKYTSAK
Description


Functional site

1) chain C
residue 821-827
type prosite
sequence AGLQFPV
description HISTONE_H2A Histone H2A signature. AGLqFPV
source prosite : PS00046

2) chain D
residue 1289-1311
type prosite
sequence REIQTAVRLLLPGELAKHAVSEG
description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
source prosite : PS00357

3) chain A
residue 466-474
type prosite
sequence PFQRLVREI
description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
source prosite : PS00959

4) chain C
residue 836
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI1

5) chain G
residue 1036
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI1

6) chain F
residue 231
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI1

7) chain F
residue 291
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI1

8) chain C
residue 874
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI2

9) chain C
residue 875
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI2

10) chain G
residue 1074
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI2

11) chain G
residue 1075
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI2

12) chain C
residue 895
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI3

13) chain G
residue 1095
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI3

14) chain C
residue 904
type MOD_RES
sequence Q
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

15) chain G
residue 1104
type MOD_RES
sequence Q
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

16) chain F
residue 251
type MOD_RES
sequence Y
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

17) chain F
residue 288
type MOD_RES
sequence Y
description N5-methylglutamine => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

18) chain C
residue 918
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

19) chain G
residue 1118
type MOD_RES
sequence K
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

20) chain E
residue 680
type MOD_RES
sequence T
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

21) chain E
residue 707
type MOD_RES
sequence T
description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
source Swiss-Prot : SWS_FT_FI5

22) chain C
residue 815
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

23) chain F
residue 277
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

24) chain C
residue 919
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

25) chain G
residue 1015
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

26) chain G
residue 1119
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

27) chain B
residue 31
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI7

28) chain F
residue 231
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI7

29) chain A
residue 522
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI8

30) chain B
residue 91
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI8

31) chain F
residue 291
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
source Swiss-Prot : SWS_FT_FI8

32) chain A
residue 510
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI9

33) chain E
residue 710
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
source Swiss-Prot : SWS_FT_FI9


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